ID A0A0P9ACP5_9CLOT Unreviewed; 396 AA.
AC A0A0P9ACP5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
GN ORFNames=OXPF_36350 {ECO:0000313|EMBL:KPU42867.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU42867.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU42867.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU42867.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPU42867.1}.
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DR EMBL; LKET01000051; KPU42867.1; -; Genomic_DNA.
DR RefSeq; WP_054876606.1; NZ_LKET01000051.1.
DR AlphaFoldDB; A0A0P9ACP5; -.
DR STRING; 36849.OXPF_36350; -.
DR PATRIC; fig|36849.3.peg.3839; -.
DR OrthoDB; 53505at2; -.
DR Proteomes; UP000050326; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KPU42867.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..236
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
SQ SEQUENCE 396 AA; 45359 MW; 570329B02593E70F CRC64;
MLQIMIFAGL MFINMAAGIF TLVLGMLGLK NLISRTPNNR LVNRLKNSAV FFMILSFVSL
GFVFYTQFAA GTPAIRDEKG SIIKDSIAEM RRIEINGRKQ WISIRGHNKN NPVILFLAGG
PGGTQMAAVR HDLKELEKYF VVVNWDQPGS GKSYYAEKVS DITPKTYIED GYVLTNYLRE
TFEQQKIFLV GESWGSALGI FLIDRYPNAY HAFVGTGQMV DFKETERIDY QKAMELAKAA
KDTDIIRKLE QNGIPPYYGD DVTWKSAVYI NYLSAYMSSD TRIHNAGYNT FRDIFSSEYG
LIDKMNYIRG IIKTFNHVYQ QLYGIDLRKD YVSLKVPVYF FEGRYDINAP LSLVEEYVNT
IDAPAKQIVW FEHSGHNPWI NESGKFVEEL KKLLPR
//
